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PLANT PHYSIOLOGY , Vol 105, Issue 4 1255-1261, Copyright © 1994 by American Society of Plant Biologists
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ENVIRONMENTAL AND STRESS PHYSIOLOGY |
A Low Molecular Mass Heat-Shock Protein Is Localized to Higher Plant Mitochondria
C. Lenne and R. Douce
Laboratoire de Physiologie Cellulaire Vegetale (Unite Associee au Centre National de la Recherche Scientifique No. 576), Departement de Biologie Moleculaire et Structurale, Centre d'Etudes Nucleaires, F-38054 Grenoble Cedex 9, France
When pea (Pisum sativum L. var Douce Provence) plants are shifted from a
normal growth temperature of 25[deg] C up to 40[deg] C for 3 h, a novel
22-kD protein is produced and accumulates in the matrix compartment of
green leaf mitochondria. HSP22 was purified and used as antigen to prepare
guinea pig antiserum. The expression of HSP22 was studied using
immunodetection methods. HSP22 is a nuclear-encoded protein de novo
synthesized in heat-stressed pea plants. The heat-shock response is rapid
and can be detected as early as 30 min after the temperature is raised. On
the other hand, HSP22 declines very slowly after pea leaves have been
transferred back to 25[deg] C. After 100 h at 25[deg] C, the heat-shock
pattern was undetectable. The precise localization of HSP22 was
investigated and we demonstrated that HSP22 was found only in mitochondria,
where it represents 1 to 2% of total matrix proteins. However, the
induction of HSP22 does not seem to be tissue specific, since the protein
was detected in green or etiolated pea leaves as well as in pea roots.
Finally, examination of matrix extracts by nondenaturing polyacrylamide gel
electrophoresis and immunoblotting with anti-HSP22 serum revealed a
high-molecular mass heat-shock protein complex of 230 kD, which contains
HSP22.
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